Small molecule–biopolymer interactions : Ultraviolet–visible and fluorescence spectroscopy and chemometrics

Ni, Yongnian, Su, Shaojing, & Kokot, Serge (2008) Small molecule–biopolymer interactions : Ultraviolet–visible and fluorescence spectroscopy and chemometrics. Analytica Chimica Acta, 628(1), pp. 49-56.

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Interactions between small molecules with biopolymers e.g. the bovine serum albumin (BSA protein), are important, and significant information is recorded in the UV–vis and fluorescence spectra of their reaction mixtures. The extraction of this information is difficult conventionally and principally because there is significant overlapping of the spectra of the three analytes in the mixture. The interaction of berberine chloride (BC) and the BSA protein provides an interesting example of such complex systems. UV–vis and fluorescence spectra of BC and BSA mixtures were investigated in pH 7.4 Tris–HCl buffer at 37 °C. Two sample series were measured by each technique: (1) [BSA] was kept constant and the [BC] was varied and (2) [BC] was kept constant and the [BSA] was varied. This produced four spectral data matrices, which were combined into one expanded spectral matrix. This was processed by the multivariate curve resolution–alternating least squares method (MCR–ALS). The results produced: (1) the extracted pure BC, BSA and the BC–BSA complex spectra from the measured heavily overlapping composite responses, (2) the concentration profiles of BC, BSA and the BC–BSA complex, which are difficult to obtain by conventional means, and (3) estimates of the number of binding sites of BC.

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ID Code: 29037
Item Type: Journal Article
Refereed: Yes
Keywords: Alternating Least Squares, Spectrofluorimetry, Ultraviolet–vis Absorbance Spectroscopy, Bovine Serum Albumin, Berberine Chloride
DOI: 10.1016/j.aca.2008.08.033
ISSN: 0003-2670
Divisions: Past > QUT Faculties & Divisions > Faculty of Science and Technology
Past > Schools > School of Physical & Chemical Sciences
Deposited On: 03 Dec 2009 05:56
Last Modified: 29 Feb 2012 13:43

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